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Database: UniProt
Entry: A0A366IPZ2_9MICO
LinkDB: A0A366IPZ2_9MICO
Original site: A0A366IPZ2_9MICO 
ID   A0A366IPZ2_9MICO        Unreviewed;       383 AA.
AC   A0A366IPZ2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
GN   ORFNames=DFO65_101139 {ECO:0000313|EMBL:RBP74421.1};
OS   Brevibacterium celere.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=225845 {ECO:0000313|EMBL:RBP74421.1, ECO:0000313|Proteomes:UP000253509};
RN   [1] {ECO:0000313|EMBL:RBP74421.1, ECO:0000313|Proteomes:UP000253509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3b_TX {ECO:0000313|EMBL:RBP74421.1,
RC   ECO:0000313|Proteomes:UP000253509};
RA   Lamendella R.;
RT   "Freshwater and sediment microbial communities from various areas in North
RT   America, analyzing microbe dynamics in response to fracking.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC         Rule:MF_01609};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RBP74421.1}.
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DR   EMBL; QNSB01000001; RBP74421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366IPZ2; -.
DR   Proteomes; UP000253509; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.590.20; -; 1.
DR   HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR011793; YbdK.
DR   NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR   PANTHER; PTHR36510; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR   PANTHER; PTHR36510:SF1; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01609, ECO:0000313|EMBL:RBP74421.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253509}.
SQ   SEQUENCE   383 AA;  42679 MW;  42CC7449BA8177C0 CRC64;
     MVDFARSPRS TIGVEWELAL IDGHSLDLAP AAEDLLAAVA EHTPDFENRI VGEMLTNTIE
     LVTGVHTDVP GIAADLSEAM ATLRTLTDPR GIELMCAGTH PFAQWQTQEI RPKDRYLELV
     DRTQWWGRNM LIYGVHVHVG IDSRDKVLPI LNALLAYVPH LQALSASSPF WGGTDTGYAS
     NRAMMFQQLP TAGLPFQFET WADYESYVED MLKTGIIDHI NEIRWDIRPS PHWGTVEVRV
     CDGVPTLEEI SALTALIQCL VDDFSARLDA GETLPTMPDW FHAENKWRAA RYGMEAIIIE
     NAAADERLVT ECLADEIERL GPTAERLGCL PELRSITALI ERGVSYQRQR EVFRTTGSLT
     EVTRSLIGDL RSSKPCAVPA DRA
//
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